ID A0A151WK30_9HYME Unreviewed; 782 AA.
AC A0A151WK30;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|RuleBase:RU362107};
DE Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU362107};
DE Flags: Fragment;
GN ORFNames=ALC60_12777 {ECO:0000313|EMBL:KYQ48222.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ48222.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ48222.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ48222.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ48222.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|ARBA:ARBA00003113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|RuleBase:RU362107};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU362107};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU362107};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU362107}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ983020; KYQ48222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151WK30; -.
DR STRING; 64791.A0A151WK30; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01578; AcnA_Mitochon_Swivel; 1.
DR CDD; cd01584; AcnA_Mitochondrial; 1.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362107};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362107};
KW Lyase {ECO:0000256|RuleBase:RU362107};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362107};
KW Mitochondrion {ECO:0000256|RuleBase:RU362107};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 66..502
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 583..710
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYQ48222.1"
SQ SEQUENCE 782 AA; 85254 MW; D5C26D8421200C6F CRC64;
LITLQKLSTL AADVQQRCFS ASPLSFAAAK VAMSKFDSTS YLPYDKLQEN LKIVKKRLNR
PLTLSEKVLY SHLDEPDKQD IVRGTSYLRL RPDRVAMQDA TAQMAMLQFI SSGLPKVAVP
STIHCDHLIE AQIGGNEDLQ RAKDINKEVY NFLKTAGAKY GVGFWNPGSG IIHQIILENY
AFPGLLMIGT DSHTPNGGGL GCLCIGVGGA DAVDVMANIP WELKCPKVIG VKLTGELKGW
TSPKDVILKV AGILTVKGGT GAIVEYFGPG VDSISCTGMA TICNMGAEIG ATTSIFPYNY
RMQDYLKATG RSEIAGAADQ HKSLLTADSN AKYDQIIELD LSTLEPHVNG PFTPDLAHPI
SKLGEVAKKN SWPNEIKVGL IGSCTNSSYE DMGRCANIAK QALKHGLKAK SAFNVTPGSE
QIRATIERDG IAQTLREFGG TVLANACGPC IGQWNRQDIK KGDKNTIVTS YNRNFTGRND
ANPATHAFVT SPELVTALSI AGKLDFNPVK DRLKGKDGKE FLLDNPYGDE LPNRGFDPGL
DTYDEPPRDG SKVKVDVDPK SQRLQLLEPF DKWDGNDLED LTILIKVKGK CTTDHISAAG
PWLKYRGHLD NISNNMFLGA VNSENGEMNK IKNQLTNEWG AVPDVARDYK KNDVKWVAVG
DENYGEGSSR EHAALEPRHL GGRAIIVKGF ARIHETNLKK QGLLPLTFSN PADYDKIQPS
DKISLLGLNN LTPGKPVQAQ IKHKDGKVDT ISLNHTMNEQ QIGWFKAGSA LNRMKEISSG
ER
//
